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The structure of a novel membrane‐associated 6‐phosphogluconate dehydrogenase from Gluconacetobacter diazotrophicus ( Gd 6PGD) reveals a subfamily of short‐chain 6PGDs
Author(s) -
SarmientoPavía Pedro D.,
RodríguezHernández Annia,
RodríguezRomero Adela,
SosaTorres Martha E.
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15472
Subject(s) - dehydrogenase , biochemistry , pentose phosphate pathway , nad+ kinase , chemistry , enzyme , biology , glycolysis
The structure of 6‐phosphogluconate dehydrogenase from Gluconacetobacter diazotrophicus ( Gd 6PGD) was determined. Active Gd 6PGD was present in both the soluble and the membrane fractions of the nitrogen‐fixing microorganism. The Gd 6PGD belongs to the newly described subfamily of short‐chain (333 AA) 6PGDs. The shorter amino acid sequence in Gd 6PGD induces the exposition of hydrophobic residues in the C‐terminal domain. This distinct structural feature is key for the protein to associate with the membrane.